Structural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectins

Maria Pia Lenza, Iker Oyenarte, Tammo Diercks, Jon Imanol Quintana, Ana Gimeno, Helena Coelho, Ana Diniz, Francesca Peccati, Sandra Delgado, Alexandre Bosch, Mikel Valle, Oscar Millet, Nicola G. A. Abrescia, Asís Palazón, Filipa Marcelo, Gonzalo Jiménez-Osés, Jesús Jiménez-Barbero, Ana Ardá, June Ereño-Orbea

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

The glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. The different possible interacting epitopes have been deeply analysed and characterized, providing evidence of the presence of glycan structures not found in previous MS-based analyses. The interaction of the RBD 13C-labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. In particular, 15N-labelled galectins (galectins-3, -7 and -8 N-terminal), Siglecs (Siglec-8, Siglec-10), and C-type lectins (DC-SIGN, MGL) have been employed. Complementary experiments from the glycoprotein perspective or from the lectin's point of view have permitted to disentangle the specific interacting epitopes in each case. Based on these findings, 3D models of the interacting complexes have been proposed.

Original languageEnglish
JournalAngewandte Chemie - International Edition
DOIs
Publication statusPublished - 21 Dec 2020

Keywords

  • glycan
  • lectin
  • molecular recognition
  • receptor binding domain
  • SARS-CoV2

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